Buried, charged, non-ion-paired aspartic acid 76 contributes favorably to the conformational stability of ribonuclease T1

Biochemistry

Volumn 38, Issue 40, 1999, Pages 13379-13384

  Giletto, Anthony ^a,b   Pace, C Nick ^a  

^a TEXAS A AND M UNIVERSITY   (United States)

^b LYNNTECH INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; RIBONUCLEASE T1;

AMINO ACID ANALYSIS; AMINO ACID SUBSTITUTION; ARTICLE; ENZYME STABILITY; ENZYME STRUCTURE; HYDROGEN BOND; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; STRUCTURE ANALYSIS;

AMINO ACID SUBSTITUTION; ASPARAGINE; ASPARTIC ACID; ELECTROSTATICS; ENZYME STABILITY; HYDROGEN-ION CONCENTRATION; IONS; MODELS, CHEMICAL; POINT MUTATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; RIBONUCLEASE T1; SERINE;

EID: 0032856161     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi991422s     Document Type: Article

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